2.400 Å
X-ray
2009-09-06
Name: | Pteridine reductase, putative |
---|---|
ID: | Q581W1_TRYB2 |
AC: | Q581W1 |
Organism: | Trypanosoma brucei brucei |
Reign: | Eukaryota |
TaxID: | 185431 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 100 % |
B-Factor: | 7.416 |
---|---|
Number of residues: | 23 |
Including | |
Standard Amino Acids: | 22 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | NAP |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.966 | 1029.375 |
% Hydrophobic | % Polar |
---|---|
43.61 | 56.39 |
According to VolSite |
HET Code: | DX6 |
---|---|
Formula: | C14H14N4O |
Molecular weight: | 254.287 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 71.23 % |
Polar Surface area: | 83.27 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 3 |
H-Bond Donors: | 3 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 3 |
X | Y | Z |
---|---|---|
36.9372 | 14.1426 | 32.594 |
Represent the protein/ligand binding mode, centered on the ligand
Dashed lines represents hydrogen bonds and metal interactions
Green residue labels for amino acids with hydrophobic contacts (green lines) to the ligand
Ligand | Protein | Interaction | |||
---|---|---|---|---|---|
Atom | Atom | Residue | Distance (Å) | Angle (°) | Type |
NAA | OG | SER- 95 | 2.95 | 167.72 | H-Bond (Ligand Donor) |
CAJ | CE1 | PHE- 97 | 4.34 | 0 | Hydrophobic |
DuAr | DuAr | PHE- 97 | 3.66 | 0 | Aromatic Face/Face |
CAD | SG | CYS- 168 | 3.42 | 0 | Hydrophobic |
NAL | OH | TYR- 174 | 2.71 | 153.3 | H-Bond (Ligand Donor) |
CAG | CD2 | LEU- 209 | 3.58 | 0 | Hydrophobic |
CAE | CE | MET- 213 | 3.58 | 0 | Hydrophobic |
CAC | CZ2 | TRP- 221 | 3.5 | 0 | Hydrophobic |
CAI | C4N | NAP- 269 | 4.05 | 0 | Hydrophobic |
CAJ | C3N | NAP- 269 | 4.05 | 0 | Hydrophobic |
NAM | O2A | NAP- 269 | 2.61 | 151.72 | H-Bond (Ligand Donor) |
NAA | O2A | NAP- 269 | 2.98 | 134.26 | H-Bond (Ligand Donor) |